ID A0A2T9YQQ1_9FUNG Unreviewed; 331 AA.
AC A0A2T9YQQ1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=Peroxin-10 {ECO:0000256|ARBA:ARBA00041230};
GN ORFNames=BB561_002355 {ECO:0000313|EMBL:PVU94675.1};
OS Smittium simulii.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133385 {ECO:0000313|EMBL:PVU94675.1, ECO:0000313|Proteomes:UP000245383};
RN [1] {ECO:0000313|EMBL:PVU94675.1, ECO:0000313|Proteomes:UP000245383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWE-8-4 {ECO:0000313|EMBL:PVU94675.1,
RC ECO:0000313|Proteomes:UP000245383};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBUNIT: Component of the PEX2-PEX10-PEX12 retrotranslocation channel,
CC composed of PEX2, PEX10 and PEX12. {ECO:0000256|ARBA:ARBA00034505}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Peroxisome
CC membrane {ECO:0000256|ARBA:ARBA00004585}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004585}.
CC -!- SIMILARITY: Belongs to the pex2/pex10/pex12 family.
CC {ECO:0000256|ARBA:ARBA00008704}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PVU94675.1}.
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DR EMBL; MBFR01000079; PVU94675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T9YQQ1; -.
DR STRING; 133385.A0A2T9YQQ1; -.
DR Proteomes; UP000245383; Unassembled WGS sequence.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016562; P:protein import into peroxisome matrix, receptor recycling; IEA:UniProt.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProt.
DR CDD; cd16527; RING-HC_PEX10; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR025654; PEX2/10.
DR InterPro; IPR006845; Pex_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23350; PEROXISOME ASSEMBLY PROTEIN 10; 1.
DR PANTHER; PTHR23350:SF0; PEROXISOME BIOGENESIS FACTOR 10; 1.
DR Pfam; PF04757; Pex2_Pex12; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Peroxisome biogenesis {ECO:0000256|ARBA:ARBA00022593};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000245383};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 279..317
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 331 AA; 36392 MW; FFEB4984675F9794 CRC64;
MEIPLDNGST ENTGVSPSTN ITQKGQAFGL PDRESQTGFE HVEATQSDLV RSSQKDSYYT
GQIYQQLSEV TSFFVGARAT AAPKQRQRLQ VISQLIYSLL TTLRGEQTLG EEYVGIMQYD
SKRNMYPSLA KRAISVLLSL FAGTMARALL KFAGKVAWPS SYDPVTLDKT VDGTVAALSR
LHLGLFYLFG RYYDLGKRLV HIELHKLRRI AQGELRSGYE LLGVLAAIQV IVAATRKTVQ
YLRARSNPSV AGPLATTKTA DKADCSKSDL NFGYSSAPCN LCLSALETPT LTACGHVFCW
ACVSEWLSSN NICPLCRQHA KQSHLILLCG Y
//